Browsing by Author "Zerihun, Yoseph"

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    Extraction and Characterization of Elastin from Raw Hide Trimmings using Autoclave Extraction Technology
    (Addis Ababa University, 2018-06) Zerihun, Yoseph; Berhanu, Assefa (PhD)
    During leather processing, raw skins/hides are trimmed and thrown as wastes and accounting for pollution load in leather industry. Elastin is a fibrous protein with multifaceted applications in biomedical field due to its intrinsic biological annotations viz elasticity and cell interactions, the extraction process is challenging task due to their cell interactive properties, the application is versatile and the price is in current international market is highly expensive. In this context, leather solid wastes specifically raw hide trimmings have been found out in the research as the potential source of raw material for elastin extraction. In this research, the raw Hide Trimming elastin content was estimated between in the range of 122 mAUmin and 97 mAUmin using the combination of FPLC, UV-Spectroscopy, SDS-PAGE protein scientific characterization techniques. The Elastin was extracted from leather waste through autoclaving technology, the method yield was found to be 90%. In addition, the biocompatibility study confirms that there is no toxic nature of extracted elastin for biological application. This implies that the selected extraction process was effective and efficient. The physical characterization using DSC result indicates that the melting peak of elastin was -0.5420 watt/g at 103.23 C, elastin showed very high denaturation temperature of 275.82 o C and TGA studies confirm that elastin have six mass loss degradation steps. The chemical characterization result using o C Solid state NMR and FTIR that elastin shows random coil, α-helix and β-strand secondary structure. Moreover, the FTIR confirm that amide A, I, II, III, IV, V, VI, and VII functional group existed in the elastin fiber. The biological characterization using amino acid analysis result show that the amino acid composition chain of the product have high amount of glycine, non-polar amino acid, low amount of acidic amino acids, low amount of hydroxyl amino acid and there is no hydroxylsine, tryptophan and Cysteine amino acids in the amino acid composition of the protein fiber. The little variations were the existence of high amount of basic amino acids in the protein amino acid composition due to the presence of collagen residues. Finally, the biocompatibility study shows that there is no toxicity nature of the extracted elastin fiber for human keratinocyte cells culture. There result is scientifically justified and confirmed that the raw hide trimmings extracted elastin makes feasible for biological and biomedical applications.